1995 Fiscal Year Final Research Report Summary
Specificity of light-harvesting systems of chromophytes in reference to their energy migration
| Project/Area Number |
06640839
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
植物生理
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
KATOH Tetsuya Kyoto Univ., Fac.Sci., Ass.Prof., 理学研究科, 助教授 (30025308)
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| Co-Investigator(Kenkyū-buntansha) |
TANAKA Ayumi Kyoto Univ., Fac.Sci., Lecturer, 理学研究科, 講師 (10197402)
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| Project Period (FY) |
1994 – 1995
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| Keywords | carotenoid / fucoxanthin / excitation energy migration / light harvesting / fucoxanthin-chlorophyll protein / brown algae / chromophyte |
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| Research Abstract |
To understand why, among a vrieties of carotenoid species, fucoxanthin is used for the light-harvesting in chromophyte algae, an attempt was made to replace the fucoxanthin molecules in fucoxanthin-chlorophyll a/c protein with different species of carotenoids and to analyze their excitation energy transfer to chlorophyll a. Treatment of purified and lyophyrized fucoxanthin-chlorophyll a/c protein from Ectocarpus (pheophyte) with anhydrous diethylether, a fucoxanthin-depleted protein preparation was obtained, in which three of 4 fucoxanthins originally bound were removed. This protein retained 2 chlorophyll a's but the excitation energy migration both between fucoxanthin and chlorophyll a between chlorophyll c and chlorophyll a were hardly seen in this protein. When this fucoxanthin-depleted protein was incubated with fucoxanthin in 0.1% lauryl sucrose, fucoxanthin was incoporated into protein in the form competent in excitation energy migration to chlorophyll a, and simultaneously regained in the energetic coupling from chlorophyll c to a. beta-Carotene and zeaxanthin were also incorporated into this protein but without showing any recovery of these energetic coupling, while neither 19'-hexanoyl oxyfucoxanthin isolated from Ruttnera (haptophyte) nor peridinin isolated from Symbionidium (dinophyte) was incorporated in this protein, indicating the fucoxanthin-binding domain of this protein is not highly specific to fucoxanthin but is not structurally fitted to modifid forms of carotenoids.
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[Publications] Osuka, A., Shinoda, S., Marumo, S., Yamada, H., Katoh, T., Yamazaki, I., Nishimura, Y., Tanaka, Y., Taniguchi, S., Okada, T., Nozaki, K.& Ohno, T.: "Fucoxanthin-pyropheophorbide and zeaxanthin-pyropheophorbide dyads as new models for study on carotenoid-chlorophyll excited state interaction" Bull.Chem.Soc.Jpn.68. 3255-3268 (1995)
Description
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[Publications] Ogata, T., Kodama, M., Nomura, S., Kobayashi., Nozawa, T., Katoh, T & Mimuro, M.: "A novel peridnin-chlorophyll a protein (PCP) from the marine dinoflagellate, Alexandrium cohorticula : a high pigment content and plural spectral forms of peridinin and chlorophyll a." FEBS Letters. 356. 367-371 (1994)
Description
「研究成果報告書概要(欧文)」より
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